Studies of structural changes in the M2 proton channel of influenza A virus by tryptophan fluorescence
Studies of structural changes in the M2 proton channel of influenza A virus by tryptophan fluorescence
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DOI：
10.1016/j.virusres.2003.10.004
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发表时间：
2004-01-01
期刊：
影响因子：
5
通讯作者：
Hay, AJ
中科院分区：
文献类型：
--
作者：
Czabotar, PE;Martin, SR;Hay, AJ
对纯化的甲型流感病毒M2蛋白的色氨酸荧光的研究已经确定了两个pH依赖性结构变化。(1)pH从8降低到6时荧光增加，涉及蛋白质N末端结构域内的色氨酸15，并且可能与通道的质子激活有关。(2)在低于pH 6时，组氨酸37使通道跨膜结构域内色氨酸41的荧光猝灭，阻断M2通道的药物可特异性逆转该猝灭。后一种效应的pH依赖性，其监测组氨酸37的质子化的变化，对应于通过通道的质子电流，并提供了组氨酸37参与质子渗透的证据。(C)2003年由Elsevier B.V.出版
Studies of tryptophan fluorescence of purified influenza A virus M2 protein have identified two pH-dependent structural changes. (1) An increase in fluorescence on reduction of pH from 8 to 6 that involves tryptophan 15 within the N-terminal domain of the protein and may be associated with proton activation of the channel. (2) Quenching of the fluorescence of tryptophan 41 within the transmembrane domain of the channel by histidine 37 below pH 6 which is specifically reversed by drugs that block the M2 channel. The pH dependence of the latter effect, which monitors changes in the protonation of histidine 37, corresponds to that of proton current through the channel and provides evidence for the involvement of histidine 37 in proton permeation. (C) 2003 Published by Elsevier B.V.